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- W2077883858 startingPage "28121" @default.
- W2077883858 abstract "Mononuclear iron enzymes can tightly bind non-activating metals. How do cells avoid mismetallation? The model bacterium Escherichia coli may control its metal pools so that thermodynamics favor the correct metallation of each enzyme. This system is disrupted, however, by superoxide and hydrogen peroxide. These species oxidize ferrous iron and thereby displace it from many iron-dependent mononuclear enzymes. Ultimately, zinc binds in its place, confers little activity, and imposes metabolic bottlenecks. Data suggest that E. coli compensates by using thiols to extract the zinc and by importing manganese to replace the catalytic iron atom. Manganese resists oxidants and provides substantial activity." @default.
- W2077883858 created "2016-06-24" @default.
- W2077883858 creator A5079628041 @default.
- W2077883858 date "2014-10-01" @default.
- W2077883858 modified "2023-10-14" @default.
- W2077883858 title "The Mismetallation of Enzymes during Oxidative Stress" @default.
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- W2077883858 doi "https://doi.org/10.1074/jbc.r114.588814" @default.
- W2077883858 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4192467" @default.
- W2077883858 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25160623" @default.
- W2077883858 hasPublicationYear "2014" @default.
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